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Interaction of CD4c Mutants with Siva-1: Insights into Cysteine Residue Functionality

This study examines the interactions of CD4c mutants (C394R/V395D and C397R) fused to LexA and Siva-1 or Lck fused to Gal4AD, analyzing histidine auxotrophy. Results indicate that both mutants successfully interact with Siva-1, suggesting that cysteine residues C394 and C397 are not essential for the interaction between CD4c and Siva-1. The findings contribute to understanding the molecular dynamics of CD4c variants and their potential roles in cellular signaling pathways.

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Interaction of CD4c Mutants with Siva-1: Insights into Cysteine Residue Functionality

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  1. LexA Hybrid Gal4AD Hybrid -His 1 CD4c C394R/V395D Gal4AD 2 CD4c C394R/V395D Lck 3 CD4c C394R/V395D Siva-1 4 CD4c C397R Gal4AD 5 CD4c C397R Lck 6 CD4c C397R Siva-1 Figure legend: L40 expressing CD4c C394R/V395D or CD4c C397R mutants fused to LexA, and Siva-1or Lck fused to Gal4AD or Gal4AD alone was analyzed for histidine auxotrophy. Both mutants are able to interact with Siva-1, demonstrating that the two cysteine residues C394 and C397 are not critical for the interaction of CD4c with Siva-1. Figure S1

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